Difference between revisions of "Phosphatase Family RTR1"

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=== Evolution ===
 
=== Evolution ===
RTR1 is found in most of eukaryotes. It is absent from Monosiga and sponge genome, though it is perhaps due to the quality of genome assembly. It is single copy in human, sea urchin, fruit fly, ''C elegans''. However, two copies are found in yeast.
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RTR1 is found in most eukaryotes. It is absent from the sponge genome, possibly due to incomplete genome assembly. It is single copy in most species including human (RPAP2). However, two copies are found in yeast (RTR1 and RTR2).
  
 
=== Domain ===
 
=== Domain ===
RTR1 has a conserved domain that carries out the phosphatase activity. Yeast RTR1 has a C-terminal region (CTR) that auto-inhibits the catalytic domain <cite>hsu14</cite>. Human RTR1 encoded by gene RPAP2 has a longer tail, but whether its function is unclear given the limited sequence similarity with CTR in yeast RTR1.
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RTR1 proteins share a conserved catalytic domain. Yeast RTR1 has a C-terminal region that auto-inhibits the catalytic domain <cite>hsu14</cite>. Human RPAP2 has a far longer tail of unknown function.
  
 
=== Function ===
 
=== Function ===
Yeast RTR1 encodes the phosphatase that dephosphorylates serine-5 of CTD repeats of RNA pol II <cite>Mosley09 kim09</cite>. These findings were challenged by later studies <cite>xiang12</cite>, but more recent study supports its activity towards serine-5 <cite>hsu14</cite>. Moreover, it has been shown that Rtr1 dephosphorylates not only serine-5 but also the newly described anti-termination tyrosine 1 marker on CTD repeats <cite>hsu14</cite>.
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Yeast RTR1 was shown to dephosphorylate serine-5 of CTD repeats of RNA pol II <cite>Mosley09 kim09</cite>. These findings were challenged by later studies <cite>xiang12</cite>, but more recent study supports its activity towards serine-5 <cite>hsu14</cite>, which also indicates that RTR1 also dephosphorylates the newly described anti-termination tyrosine 1 residue of CTD repeats <cite>hsu14</cite>.
  
 
=== References ===
 
=== References ===

Revision as of 00:13, 23 March 2015

Phosphatase Classification: Fold RTR1: Superfamily RTR1: Family RTR1

RTR1 is a phosphatase conserved in eukaryotes that regulates the phosphorylation states of C-terminal domain (CTD) of RNA polymerase II.

Evolution

RTR1 is found in most eukaryotes. It is absent from the sponge genome, possibly due to incomplete genome assembly. It is single copy in most species including human (RPAP2). However, two copies are found in yeast (RTR1 and RTR2).

Domain

RTR1 proteins share a conserved catalytic domain. Yeast RTR1 has a C-terminal region that auto-inhibits the catalytic domain [1]. Human RPAP2 has a far longer tail of unknown function.

Function

Yeast RTR1 was shown to dephosphorylate serine-5 of CTD repeats of RNA pol II [2, 3]. These findings were challenged by later studies [4], but more recent study supports its activity towards serine-5 [1], which also indicates that RTR1 also dephosphorylates the newly described anti-termination tyrosine 1 residue of CTD repeats [1].

References

  1. Hsu PL, Yang F, Smith-Kinnaman W, Yang W, Song JE, Mosley AL, and Varani G. Rtr1 is a dual specificity phosphatase that dephosphorylates Tyr1 and Ser5 on the RNA polymerase II CTD. J Mol Biol. 2014 Aug 12;426(16):2970-81. DOI:10.1016/j.jmb.2014.06.010 | PubMed ID:24951832 | HubMed [hsu14]
  2. Mosley AL, Pattenden SG, Carey M, Venkatesh S, Gilmore JM, Florens L, Workman JL, and Washburn MP. Rtr1 is a CTD phosphatase that regulates RNA polymerase II during the transition from serine 5 to serine 2 phosphorylation. Mol Cell. 2009 Apr 24;34(2):168-78. DOI:10.1016/j.molcel.2009.02.025 | PubMed ID:19394294 | HubMed [Mosley09]
  3. Xiang K, Manley JL, and Tong L. The yeast regulator of transcription protein Rtr1 lacks an active site and phosphatase activity. Nat Commun. 2012 Jul 10;3:946. DOI:10.1038/ncomms1947 | PubMed ID:22781759 | HubMed [xiang12]
  4. Kim M, Suh H, Cho EJ, and Buratowski S. Phosphorylation of the yeast Rpb1 C-terminal domain at serines 2, 5, and 7. J Biol Chem. 2009 Sep 25;284(39):26421-6. DOI:10.1074/jbc.M109.028993 | PubMed ID:19679665 | HubMed [Kim09]
All Medline abstracts: PubMed | HubMed